Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.2.1.36 (hyaluronidase)
 4,606 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Mycobacterium ulcerans produces an exotoxin in culture which, when inoculated into guinea pig skin, causes inflammation, necrosis, edema, and other histopathological changes resembling those in infections of humans. The toxin was resistant to heat and to alkalies and was moderately acid labile. Toxic activity was destroyed by Pronase, phospholipase, lipase, amylase, and glucosidase but not by trypsin, collagenase, cellulase, lysozyme, hyaluronidase, or neuraminidase. Toxic activity was resistant to treatment with 2-mercaptoethanol, urea, guanidine hydrochloride, p-chloromercuribenzoate, ethylenediaminetetraacetate, and sodium deoxycholate but was destroyed by sodium m-periodate and sodium dodecyl sulfate. The toxin was precipitated by a wide range of ammonium sulfate concentrations. Extraction with chlorofrom-methanol or petroleum ether destroyed its activity. Isopycnic density gradient ultracentrifugation in KBr produced a high-density lipoprotein layer with a 24-fold increase in specific activity. The results indicate that this toxin is a high-molecular-weight phospholipoprotein-polysaccharide complex.
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PMID:Further characterization of Mycobacterium ulcerans toxin. 3 Jun 94

Current knowledge of the pathophysiology of bacterial infections is elementary. Thie initial events leading to the invasion of host tissues are a matter of conjecture for many bacterial organisms. This is particularly true for pneumococci, the most frequent causative organisms of acute otitis media. Bacterial enzymes may account for the initial disruption of host tissues, and this study explored their role in the infectious process. As first step, pneumococcal cultures were analyzed, and significant levels of the enzymes lipase and hyaluronidase were demonstrated. Secondly, the presence of these enzymes in middle ear effusions was explored in an animal model of acute otitis media. The enzymes reached peak levels at seven days. The third and most important portion of the study examined the significance of these enzymes in producing inflammation and alterations in the middle ear cavity of normal experimental animals. This portion was a histologic comparison of temporal bone specimens and demonstrated that marked acute and chronic changes can be induced by placing solutions of these enzymes in the middle ear cavity. This study concludes that bacterial enzymes play an important role in the induction of acute otitis media.
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PMID:The role of bacterial enzymes in inducing inflammation in the middle ear cavity. 4 3

The ultrastructural study of liver tissues from 38 patients with type B viral hepatitis consistently showed the presence of hepatitis B core antigen of 21-25 nm size in the liver cell nuclei and to a lesser extent in the cytoplasm. This finding and the demonstration of the tubular form of hepatitis B surface antigen in the proliferative degranulated endoplasmic reticulum constituted the etiologic criterion for the diagnosis of the disease. The double-shelled Dane-like particles were frequently found in association with the tubular form of the surface antigen. The core particles were found in the protoplasmic processes of hepatocytes and this correlated with the immunofluorescent microscopic findings that the antigen may be shed into circulation with the protoplasm. The core antigen was found to resist digestion by various enzymes such as protease, DNase, RNase, phospholipase C, lipase, lysozyme, diastase, neuraminidase and hyaluronidase, all of which did not destroy the immunoreactivity as demonstrated by immunoelectron and immunofluorescent microscopy. Similarly, sodium dodecyl sulfate, Tween 80 and mercaptoethanol also had no effect. The formalin-fixed paraffin-embedded liver tissue sections could be treated with protease to facilitate the immunofluorescent staining for the core antigen in tissue.
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PMID:Structural and immunoreactive characteristics of hepatitis B core antigen. 5 6

The ascites form of a chemically induced guinea pig hepatoma, line-10, was resistant to killing in vitro by xenogeneic antibody and guinea pig complement. Pretreatment of line-10 cells with certain proteolytic enzymes rendered tham susceptible to the killing action of antibody and guinea pig complement. The effects of enzyme pretreatment were dependent on enzyme concentration, temperature, and could be blocked by addition of competitive or non-competitive inhibitors. The effect of the enzyme treatment could reversed by incubating the treated cells at 37 degrees C (but not at 0 degrees C), in the absence of the enzyme. Effective enzymes included ficin, bromelain, pronase, elastase, papain, trypsin, collagenase, lipases type I and type VI, and the neuraminidase preparation isolated from Clostridium perfringens. The activity of the lipase preparations and the neuraminidase preparation isolated from Clostridium perfringens appeared to be caused by proteolytic enzyme contamination. Enzyme preparations that proved ineffecitve in rendering the line-10 cells sensitive to killing by antibody and guinea pig complement included DNase, RNase, beta-glucuronidase type 6A or type B10, hyaluronidase type V or type VI, and pectinesterase.
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PMID:Lysis of tumor cells by antibody and complement. VI. Enhanced killing of enzyme-pretreated tumor cells. 17 70

Optimal conditions for detecting staphylokinase, phosphatase, protease, lipase, esterase, egg yolk factor, lysozyme, deoxyribonuclease, hyaluronidase, penicillinase, and alpha-, beta-, and delta-hemolysins in cell-free filtrates of selected strains of staphylococci by agar plate methods were established by studying the effect of factors such as buffer composition, pH, ionic strength, type of agar, nature and concentration of substrate, and certain metal ions. The final tests that evolved from this study are simple to perform, require only 6 mul of the sample per test, and are capable of detecting microgram and, in some cases, nanogram quantities of the product. The zones of reaction can also be quantitatively related to the amount of material present. The test may also be useful for the detection of extracellular products of other microorganisms.
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PMID:Agar plate tests of enhanced sensitivity for detecting biologically active products of staphylococcal filtrates. 18 61

The extracellular production of hyaluronidase and chondroitin sulfatase was demonstrated in all of the subspecies of Bacteroides fragilis tested with the exception of B. fragilis subsp. vulgatus. Elastase was found only in one strain of B. coagulans tested. This appears to be the first report of these enzyme activities in this genus. Additional enzymes found to be produced by certain members othis genus were fibrinolysin, penicillinase, lysozyme, lecithinase, deoxyribonuclease, phosphatase, protease, and lipase.
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PMID:Extracellular enzymes of the genus Bacteroides. 18 84

Three methods at present available for the purification of staphylococcal delta-haemolysin were compared as to the purity and identify of the product obtained. None yielded a pure preparation of delta-haemolysin; one of the three preparations did not contain demonstrable delta-haemolysin when tested electrophoretically, but it contained deoxyribonuclease, penicillinase, phosphatase and alpha-haemolysin. The second preparation had delta-haemolysin activity and was free of alpha-haemolysin, but it contained lipase, egg-yolk factor, esterase, deoxyribonuclease, penicillinase, phosphatase and hyaluronidase. The third preparation contained all of the products mentioned above, except phosphatase, and it also contained alpha-haemolysin, staphylokinase, lysozyme and caseinase. These findings are discussed with special reference to the requirement for criteria of purity in work with staphylococcal products.
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PMID:Purity of staphylococcal delta-haemolysin obtained by three different procedures. 18 51

The mammalian toxicity of the potently algogenic venom of the ant Pogonomyrmex badius is greater than that reported for any other insect venom. This enzyme-rich venom contains high concentrations of phospholipase A2 and B, hyaluronidase, acid phosphatase, lipase, and esterases. This hemolytic secretion from the poison gland products unusual symptoms in mammals and appears to have been evolved as a deterrent for vertebrate predators.
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PMID:A harvester ant venom: chemistry and pharmacology. 65 54

The release of beta-lysin, which followed the intravenous injection of antigen-antibody complexes, did not take place when these complexes were added to citrated whole blood but did occur in heparinized blood. beta-Lysin release in heparinized blood was inhibited by citrate but were reversed by the addition of calcium ions that implicated complement reactions. Fourteen different enzymes were added to platelet-rich plasma (PRP). Streptokinase, neuraminidase, papain, phospholipase C, sulfatase, and trypsin caused platelets to release significant quantities of beta-lysin, whereas elastase, phosphatase, protease, ribonuclease A, hyaluronidase, lipase, and pepsin caused little or no increase in the plasma beta-lysin concentration. One enzyme, fibrinolysin, inactivated beta-lysin faster than it was released. The enzyme-induced release of beta-lysin from PRP was often accompanied by a reduction in the number of platelets. The intravenous injection of streptokinase, neuraminidase, and sulfatase caused in vivo releases of beta-lysin into the plasma. The platelet-aggregating substances collagen, arachidonic acid, and adenosine 5'-diphosphate caused beta-lysin to be released from PRP. The platelet-aggregating substances L-epinephrine, zymosan, fibrinogen, reserpine, and serotonin caused little or no release of beta-lysin from platelets. The results of this study indicate that the release of beta-lysin during antigen-antibody-complement reactions, blood coagulation, phagocytosis, and inflammation could be enzyme mediated.
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PMID:Release of beta-lysin from platelets caused by antigen-antibody complexes, purified enzymes, and platelet-aggregating substances. 84 4

Cholerogen-toxoid served as a complex vaccine preparation composed of the main pathogenicity factors of cholera vibrio--cholerogen (toxoid), endotoxin and a number of exoenzymes. The preparation contains 65 +/- 7.5% of protein, 12 +/- 1.2% of reducing sugars, 7 +/- 1.2% of lipids, and 2 +/- 0.3% of nucleic acids. Analytic disc-electrophoresis in polyacrylamide gel and immune disc-electrophoresis revealed at least seven individual proteins with the serological activity in the preparation. About 70% of these constituted toxoid proper; the content of O-antigen was 22%. In the cholerogen-toxoid there were revealed seven exoenzymes of cholera vibrio; proteinase, lecithinase, lipase, DNA-ase, RNA-ase, hyaluronidase, amylase. Antibodies against proteinase, lecithinase, amylase and RNA-ase of cholera vibrio were found in the serum of rabbits immunized with cholerogen-toxoid.
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PMID:[Immunochemical and biochemical characteristics of a preventive preparation against cholera, cholerogen-toxoid]. 94 1


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